NU1C_CHAGL
ID NU1C_CHAGL Reviewed; 363 AA.
AC Q8M9T6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01350};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NAD(P)H dehydrogenase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE Short=NDH subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
GN Name=ndhA {ECO:0000255|HAMAP-Rule:MF_01350};
OS Chaetosphaeridium globosum (Charophycean green alga) (Herposteiron
OS globosum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Coleochaetophyceae; Coleochaetales;
OC Chaetosphaeridiaceae; Chaetosphaeridium.
OX NCBI_TaxID=96477;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1311;
RX PubMed=12161560; DOI=10.1073/pnas.162203299;
RA Turmel M., Otis C., Lemieux C.;
RT "The chloroplast and mitochondrial genome sequences of the charophyte
RT Chaetosphaeridium globosum: insights into the timing of the events that
RT restructured organelle DNAs within the green algal lineage that led to land
RT plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11275-11280(2002).
CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC and possibly in a chloroplast respiratory chain. The immediate electron
CC acceptor for the enzyme in this species is believed to be
CC plastoquinone. Couples the redox reaction to proton translocation, and
CC thus conserves the redox energy in a proton gradient.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01350};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01350};
CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01350}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR EMBL; AF494278; AAM96514.1; -; Genomic_DNA.
DR RefSeq; NP_683857.1; NC_004115.1.
DR AlphaFoldDB; Q8M9T6; -.
DR SMR; Q8M9T6; -.
DR GeneID; 860797; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01350; NDH1_NuoH; 1.
DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR PANTHER; PTHR11432; PTHR11432; 1.
DR Pfam; PF00146; NADHdh; 1.
DR PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Thylakoid; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..363
FT /note="NAD(P)H-quinone oxidoreductase subunit 1,
FT chloroplastic"
FT /id="PRO_0000240017"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 363 AA; 39601 MW; 8C103CEC4B0DF529 CRC64;
MDLNEKIINI LSSVGLTKNL SIFILDLIPI LIILLGATLG VLVIVWLERK ISAAVQQRIG
PEYAGPLGMI QALADGLKLV LKEDIIPAKG DPWLFSVGPA LVVVPVFLSY LVVPFGHELI
LANLGVGILF WIALSSIAPL GLLMAGYGSN NKYSFLGGLR AAAQAISYEI PLALCVLSVA
LLSHSLSTVD IVEEQSKYGI LGWNIWRQPI GFIAFLIASL AECERLPFDL PEAEEELVAG
YQTEYCGIKF GLFYVGSYLN LLVSALFVSV LYLGGWNFSL PWINFPILLT ENDFALSLNI
VNATLGIAIT LGKAYLFLFL SILARWTLPR VRMDQLLDLG WKFLLPVSLG NLLLTASLQL
ALL
